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3mzo

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of a HD-domain phosphohydrolase (lin2634) from LISTERIA INNOCUA at 1.98 A resolution. To be published
    Site JCSG
    PDB Id 3mzo Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS25775,NP_471964.1, _0077.001156_
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.32 Rfactor 0.166
    Waters
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    Solvent Content 47.07

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 3mzo

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    Protein Summary

    Lin2634 (Fig.1) from is likely a  HD-domain phosphohydrolase (PFAM PF01966), it has 24% seq id with  YfbR from Escherichia coli [Ref], which is a 5'-deoxyribonucleotidase (pdb 2paq). The two structures can be superimposed with a rmsd of 2.3A for 170 aligned Ca. The active site (Arg18, His33, Asp137, His67 etc) is also very similar. However, the residues at the perimeter is not conserved, suggesting possible difference in substrate specificity. It is likely Lin2634 functions as a hexamer (Fig 2).

     

    Two calcium ions from crystallization conditions are present in the putative metal binding sites (Fig 1).

     

    Fig. 1. Structure of Lin2634

    mh11582f-mono.png

    Fig. 2. Hexamer of Lin2634 (2 views, rotate around x by 90)

    mh11582f-hex1.pngmh11582f-hex2.png

    Ligand Summary

    Reviews

    References

     

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    Files (3)

    FileSizeDateAttached by 
     mh11582f-hex1.png
    MH11582F hexamer view 1
    219.51 kB19:49, 15 Apr 2010qxuActions
     mh11582f-hex2.png
    MH11582F hexamer view 2
    219.78 kB19:49, 15 Apr 2010qxuActions
     mh11582f-mono.png
    MH11582F monomer
    139.49 kB19:49, 15 Apr 2010qxuActions
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